Source:http://linkedlifedata.com/resource/pubmed/id/20923667
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
|
pubmed:dateCreated |
2010-10-6
|
pubmed:abstractText |
The use of nondestructive NMR spectroscopy for enzymatic studies offers unique opportunities to identify nearly all enzymatic byproducts and detect unstable short-lived products or intermediates at the molecular level; however, numerous challenges must be overcome before it can become a widely used tool. The biosynthesis of acetyl-coenzyme A (acetyl-CoA) by acetyl-CoA synthetase is used here as a case study for the development of an analytical NMR-based time-course assay platform. We describe an algorithm to deconvolve superimposed spectra into spectra for individual molecules, and further develop a model to simulate the acetyl-CoA synthetase enzyme reaction network using the data derived from time-course NMR. Simulation shows indirectly that synthesis of acetyl-CoA is mediated via an enzyme-bound intermediate (possibly acetyl-AMP) and is accompanied by a nonproductive loss from an intermediate. The ability to predict enzyme function based on partial knowledge of the enzymatic pathway topology is also discussed.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Oct
|
pubmed:issn |
1542-0086
|
pubmed:author | |
pubmed:copyrightInfo |
Copyright © 2010 Biophysical Society. Published by Elsevier Inc. All rights reserved.
|
pubmed:issnType |
Electronic
|
pubmed:day |
6
|
pubmed:volume |
99
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
2318-26
|
pubmed:dateRevised |
2011-10-19
|
pubmed:meshHeading |
pubmed-meshheading:20923667-Acetate-CoA Ligase,
pubmed-meshheading:20923667-Algorithms,
pubmed-meshheading:20923667-Arabidopsis,
pubmed-meshheading:20923667-Biocatalysis,
pubmed-meshheading:20923667-Least-Squares Analysis,
pubmed-meshheading:20923667-Magnetic Resonance Spectroscopy,
pubmed-meshheading:20923667-Multienzyme Complexes,
pubmed-meshheading:20923667-Time Factors
|
pubmed:year |
2010
|
pubmed:articleTitle |
Time-resolved NMR: extracting the topology of complex enzyme networks.
|
pubmed:affiliation |
Complex Carbohydrate Research Center, University of Georgia, Athens, GA, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
|